β-amyloid ,

Amyloid β Peptide (42-1)(human) acetate is the inactive form of Amyloid β Peptide (1-42). Amyloid β Peptide (42-1)(human) acetate is a 42-amino acid peptide which plays a key role in the pathogenesis of Alzheimer disease.

β-Amyloid (1-42), acetate (human) is a peptide consisting of 42 amino acids that is part of β-Amyloid and is commonly used in Alzheimer's disease modeling.

β-Amyloid 15-21 acetate (Beta-Amyloid (15-21) acetate) is a fragment of Amyloid-β peptide, maybe used in the research of neurological disease. This fragment is involved in beta sheet formation.

β-amyloid 1-11 acetate is a fragment of Amyloid-β peptide, maybe used in the research of neurological disease.

Amyloid β-Protein 10-20 acetate (Amyloid β-Protein 10-20 acetate (152286-31-2 free base)) is a fragment of Amyloid-β peptide, maybe used in the research of neurological disease.Amyloid β protein fragment containing the α-secretase processing site (Lys16-Leu17 bond). It also contains the HHQK domain (residues 13-16) responsible for binding to microglial cells.

Biotin-β-Amyloid (1-42), human TFA, also known as Biotin-Amyloid β-Peptide (1-42) (human) TFA, is a biotin-labeled 42-amino acid peptide implicated in the pathogenesis of Alzheimer's disease.

β-Amyloid (1-42), human, is a 42-amino acid peptide integral to the pathogenesis of Alzheimer disease.

β-Amyloid (31-35) (β-Amyloid 31-35) is the shortest sequence of native Amyloid-β peptide.

Amyloid-β (25-35) (Aβ (25-35)) is an 11-residue fragment of the Aβ protein that retains the physical and biological characteristics of the full length peptide. It forms fibrils that react to thioflavin T and Congo red and are organized in a cross-β arrangement of β-strands similar to Aβ (1-40) and Aβ (1-42) fibrils. Aggregated Aβ (25-35) decreases the viability of rat adrenal PC12 cells. It also decreases the viability of primary rat cortical neurons at concentrations ranging from 1 nM to 30 μM. In vivo, intracerebral injection of Aβ (25-35) (20 nmol) in rats induces lesions of neuronal and tissue loss. Aggregated Aβ (25-35) administered intracerebroventricularly to rats induces learning and memory impairments in the Y-maze, novel object recognition, and contextual fear conditioning tests.

β-Amyloid peptide(16-20), with the amino acid sequence (KLVFF) derived from Amyloid-β (Abeta), functions as an efficient inhibitor of Abeta fibril formation. This compound is modified with RG-/-GR-NH2 residues at both its N- and C-terminal ends to enhance solubility [1].

Rat form of the beta-Amyloid (1-40) peptide

β-Amyloid (29-40) is a fragment of Amyloid-β peptide. Alzheimer's beta amyloid peptide (29-40 42) C-terminal fragments exhibit physical and chemical properties similar to fusion peptides of viral proteins, inducing liposome fusion in vitro.

β-Amyloid (1-16) is an amyloidogenic protein fragment derived from the β-amyloid sequence, known for its ability to bind metal ions, indicating its role in metal-binding processes. β-Amyloid, a peptide, is responsible for forming amyloid plaques in the brains of people with Alzheimer's disease (AD).

(Nle35)-Amyloid β-Protein (1-42) ammonium is a peptide.

β-Amyloid (22-35) is a 14-aa peptide, shows aggregates and induces neurotoxicity in the hippocampal cells. Beta amyloid (22-35) is a synthetic truncated fragment of beta-amyloid peptide.

β-Amyloid (1-40), England mutation, is a biologically active peptide with a histidine (His) to arginine (Arg) substitution at position 6, known to enhance oligomerization kinetics that serve as fibril seeds and increase neurotoxicity in cultured neurons. This alteration is one of several mutations in the beta-amyloid precursor gene implicated in autosomal dominant Alzheimer's Disease across multiple kindreds.

(Gln22,Asn23)-Amyloid β-Protein (1-40) is a peptide used to study Cerebral Amyloid Angiopathy Mutations [1].

Cys-Gly-Lys-Arg-Amyloid β-Protein (1-42), a peptide fragment derived from amyloid β-protein (Aβ), is crucial in Alzheimer's disease research [1].

Antibodies corresponding to beta-amyloid (4-10) are effective in vivo inhibitors of cytotoxicity, amyloid plaque formation and special memory disturbances in mice. This peptide does not elicit an inflammatory response.

Amyloid β-Protein (10-20) is a fragment of Amyloid-β peptide, maybe used in the research of neurological disease.Amyloid β protein fragment containing the α-secretase processing site (Lys16-Leu17 bond). It also contains the HHQK domain (residues 13-16) re

β-Amyloid (1-16) rat is a fragment of the amyloid beta (Abeta) peptide's metal-binding domain, containing three amino acid substitutions compared to its human counterpart, which confer reduced susceptibility to Alzheimer's disease-like neurodegeneration in rats and mice [1].

β-Amyloid (1-42), rat TFA is a 42-aa peptide, shows the effects of cytotoxicity on acute hippocampal slices, and has been used in studies of alzheimer's disease.

Beta-Amyloid Protein Precursor 770 (135-155)Aβ Protein Precursor 770 (135-155)

β-Amyloid (1-15) (Amyloid β-Protein (1-15)) is a fragment of β-amyloid protein used in the study of Alzheimer's disease.

(Gly22)-Amyloid β-Protein (1-42), a peptide fragment of Amyloid β-Protein (Aβ), plays a crucial role in Alzheimer's disease by forming the main component of vascular and parenchymal amyloid deposits. The Glu22 to Gly22 mutation in Aβ is known to enhance aggregation [1] [2].

Anionic interaction of Beta-amyloid (1-11) with Factor XII is suspected to cause massive activation of the C4 (complement 4) system in the cerebrospinal fluid of Alzheimer’s disease patients.

β-Amyloid 22-35 (Amyloid β-Protein 22-35) TFA, a fragment comprising residues 22-35 of the β-amyloid protein, exhibits cytotoxicity towards cultured rat hippocampal neurons in serum-free media. It aggregates and forms typical amyloid fibrils in neutral buffer solution, mirroring those observed with the full-length β-amyloid protein [1].

β-Amyloid (42-1), human TFA, a 42-amino acid peptide, represents the inactive form of Amyloid β Peptide (1-42) and is crucial in the development of Alzheimer's disease [1].

β-Amyloid (1-40) TFA, a principal protein in plaques observed in the brains of Alzheimer's disease patients [1], is pivotal in research focused on this neurodegenerative disorder.

β-Amyloid (1-40), FAM-labeled, is a β-Amyloid (1-40) peptide tagged with a FAM fluorescent label, exhibiting an excitation wavelength (λ ex) of 492 nm and an emission wavelength (λ em) of 518 nm.

'(Lys22)-Amyloid β-Protein (1-42) represents a mutation of the wild-type (WT) Amyloid β-Protein (1-42) peptide [1].'

[Ala28]-β Amyloid(25-35) (β(25-35)KA), an electrically neutral mutant variant of Aβ(25-35), facilitates the accelerated aggregation of Firefly Luciferase [1].

[Arg6]-β-Amyloid (1-42), England mutation, is a biologically active peptide linked to autosomal dominant Alzheimer's Disease in various kindreds. The English (H6R) mutation disrupts H6 interactions due to alterations in the beta-amyloid precursor gene.

β-Amyloid (1-40), FAM-labeled TFA, is a FAM fluorescently-labeled β-Amyloid (1-40) peptide (λ ex = 492 nm and λ em = 518 nm) [1].

β-Amyloid precursor protein (96-110), cyclized (human), a segment of the amyloid precursor protein, serves as a research tool in Alzheimer's disease studies [1].

Acetyl-β Amyloid (15-20), Amide is a peptide fragment that inhibits β-sheet formation and stabilizes the structure of the Aβ (1–40) peptide, making it a useful tool in Alzheimer’s disease research [1].

(Pyr11)-Amyloid β-Protein (11-40) (Aβ11pE-40), a peptide, is utilized in Alzheimer's disease research [1].

β-Amyloid (1-14), mouse, rat, is a 1-14 fragment of the Amyloid-β peptide.

Amyloid β-Protein (3-42), the precursor of Pyr peptide, serves as the foundation of the amyloid template block in Alzheimer's disease when modified to pyroglutamate Aβ (pEAβ) (3-42). This modified form, pEAβ(3-42), hastens the aggregation of Aβ(1-42) although Aβ(1-42) markedly decelerates both the primary and secondary nucleation of pEAβ(3-42) [1].

(Met(O2)35)-Amyloid β-Protein (1-42) is a peptide [1].

β-Amyloid (33-40) is a peptide composed of amino acids 33 to 40 from the beta-amyloid protein.

β-Amyloid (35-42), a peptide derived from the beta-amyloid protein, encompasses amino acids 35 through 42.

β-amyloid (15-21) is a fragment of Amyloid-β peptide, maybe used in the research of neurological disease. This fragment is involved in beta sheet formation.

β-Amyloid (11-22) is a peptide fragment of β-Amyloid. β-Amyloid peptide (Abeta), the primary component of amyloid plaques in the brains of Alzheimer’s patients, is believed to be the cause of Alzheimer’s Disease (AD), the most common neurodegenerative disease, affecting approximately 10% of the population over 60.

β-Amyloid (1-43)(human) TFA exhibits greater aggregation tendencies and heightened toxicity compared to Aβ1-42. This compound also associates with sAPPα and sAPPβ and has the potential to serve as an additional biomarker for Alzheimer’s disease (AD), complementing existing markers [1].

(Met(O)35)-Amyloid β-Protein (1-42) is the oxidized form of Methionine 35 in Aβ42, capable of producing an oligomer size distribution similar to Aβ40. This compound is utilized in Alzheimer’s disease (AD) research [1].

β-Amyloid (1-38), derived from mice and rats, is a chemical compound comprising 38 amino acids, specifically residues 1-38 of the Aβ peptide. Notably, it serves as the primary constituent of amyloid plaques associated with Alzheimer's disease.

Biotinyl-Ahx-Amyloid β-Protein (1-42) ammonium is an N-terminally biotin-tagged form of Amyloid β-Protein (1-42), the primary component of vascular and parenchymal amyloid deposits associated with Alzheimer's disease [1].

(Gln22)-Amyloid β-Protein (1-42), a Dutch mutation (E22Q) variant of β-Amyloid (1-42), exhibits enhanced fibrillogenic and pathogenic properties [1].

This synthetic peptide consists of amino acids 1 to 17 of beta amyloid protein. This peptide can be employed in beta amyloid solubility studies.